Overexpression, purification, crystallization and preliminary X-ray crystal analysis of Bacillus pallidusD-arabinose isomerase.
D-Arabinose isomerase catalyzes the isomerization of D-arabinose to D-ribulose. Bacillus pallidus D-arabinose isomerase has broad substrate specificity and can catalyze the isomerization of D-arabinose, L-fucose, L-xylose, L-galactose and D-altrose. Recombinant B. pallidus D-arabinose isomerase was overexpressed, purified and crystallized. A crystal of the enzyme was obtained by the sitting-drop method at room temperature and belonged to the orthorhombic space group P2(1)2(1)2, with unit-cell parameters a = 144.9, b = 127.9, c = 109.5 A. Diffraction data were collected to 2.3 A resolution.
Takeda
Kosei
K
Division of Structural Biology, Life Science Research Center and Faculty of Medicine, Kagawa University, 1750-1 Ikenobe, Miki-cho, Kita-gun, Kagawa 761-0793, Japan.
Yoshida
Hiromi
H
Takada
Goro
G
Izumori
Ken
K
Kamitori
Shigehiro
S
D019747:Aldose-Ketose Isomerases / Q000737:chemistry / Q000235:genetics* / Q000302:isolation & purification / Q000378:metabolism; D001407:Bacillus / Q000201:enzymology*; D001426:Bacterial Proteins / Q000737:chemistry / Q000235:genetics* / Q000302:isolation & purification; D018360:Crystallography, X-Ray / Q000379:methods; D017931:DNA Primers; D010429:Pentoses / Q000378:metabolism; D016133:Polymerase Chain Reaction
D001426:Bacterial Proteins; D017931:DNA Primers; D010429:Pentoses; C100182:ribulose; D019747:Aldose-Ketose Isomerases; C019714:D-arabinose isomerase